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Literature summary for 1.1.1.430 extracted from

  • Pival, S.L.; Klimacek, M.; Nidetzky, B.
    The catalytic mechanism of NADH-dependent reduction of 9,10-phenanthrenequinone by Candida tenuis xylose reductase reveals plasticity in an aldo-keto reductase active site (2009), Biochem. J., 421, 43-49.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H113A mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s Yamadazyma tenuis
L80A mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s Yamadazyma tenuis
Y51A mutation causes a 10000-100000fold decrease in the rate constant for hydride transfer from NADH to 9,10-phenanthrenequinone, whose value in the wild-type enzyme is about 800 per s Yamadazyma tenuis

Organism

Organism UniProt Comment Textmining
Yamadazyma tenuis O74237
-
-

Reaction

Reaction Comment Organism Reaction ID
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+ enzymic mechanism in which a catalytic proton bridge from the protonated side chain of Lys80 to the carbonyl group adjacent to the hydride acceptor carbonyl facilitates the chemical reaction step. His113 contributes to positioning of the 9,10-phenanthrenequinone substrate for catalysis. Tyr51 controls release of the hydroquinone product. The proposed chemistry involves delivery of both hydrogens required for reduction of the alpha-dicarbonyl substrate to the carbonyl group undergoing stereoselective transformation. Hydride transfer from NADH probably precedes the transfer of a proton from Tyr51 Yamadazyma tenuis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
9,10-phenanthrenequinone + NADPH + H+
-
 Yamadazyma tenuis ? + NADP+
-
 ?
D-xylose + NADPH + H+
-
 Yamadazyma tenuis xylitol + NADP+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.002
-
 D-xylose mutant K80A, pH 7.0, 25°C Yamadazyma tenuis
0.02
-
 D-xylose mutant H113A, pH 7.0, 25°C Yamadazyma tenuis
0.027
-
 9,10-phenanthrenequinone mutant K80A, pH 7.0, 25°C Yamadazyma tenuis
0.043
-
 9,10-phenanthrenequinone mutant H113A, pH 7.0, 25°C Yamadazyma tenuis
0.2
-
 9,10-phenanthrenequinone mutant Y51A, pH 7.0, 25°C Yamadazyma tenuis
10
-
 D-xylose wild-type, pH 7.0, 25°C Yamadazyma tenuis
12
-
 9,10-phenanthrenequinone wild-type, pH 7.0, 25°C Yamadazyma tenuis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0009
-
 D-xylose mutant K80A, pH 7.0, 25°C Yamadazyma tenuis
0.2
-
 D-xylose mutant H113A, pH 7.0, 25°C Yamadazyma tenuis
20
-
 9,10-phenanthrenequinone mutant H113A, pH 7.0, 25°C Yamadazyma tenuis
33
-
 9,10-phenanthrenequinone mutant Y51A, pH 7.0, 25°C Yamadazyma tenuis
500
-
 9,10-phenanthrenequinone mutant K80A, pH 7.0, 25°C Yamadazyma tenuis
2300
-
 9,10-phenanthrenequinone wild-type, pH 7.0, 25°C Yamadazyma tenuis